Functional dynamics in the active site of the ribonuclease binase.

@article{Wang2001FunctionalDI,
  title={Functional dynamics in the active site of the ribonuclease binase.},
  author={L D Wang and Y Pang and Tina M Holder and Jeffrey R. Brender and Alexander Kurochkin and Erik R.P. Zuiderweg},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2001},
  volume={98 14},
  pages={7684-9}
}
Binase, a member of a family of microbial guanyl-specific ribonucleases, catalyzes the endonucleotic cleavage of single-stranded RNA. It shares 82% amino acid identity with the well-studied protein barnase. We used NMR spectroscopy to study the millisecond dynamics of this small enzyme, using several methods including the measurement of residual dipolar couplings in solution. Our data show that the active site of binase is flanked by loops that are flexible at the 300-micros time scale. One of… CONTINUE READING

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